Log in to save to my catalogue

Structural basis of tubulin detyrosination by VASH2/SVBP heterodimer

Structural basis of tubulin detyrosination by VASH2/SVBP heterodimer

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_73149a2dc2634b788e4b85463c6af74a

Structural basis of tubulin detyrosination by VASH2/SVBP heterodimer

About this item

Full title

Structural basis of tubulin detyrosination by VASH2/SVBP heterodimer

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2019-07, Vol.10 (1), p.3212-8, Article 3212

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The C-terminus of α-tubulin undergoes a detyrosination/tyrosination cycle and dysregulation of this cycle is associated with cancer and other diseases. The molecular mechanisms of tubulin tyrosination are well studied, however it has remained unknown how tyrosine is cleaved from the tubulin tail. Here, we report the crystal structure of the long-so...

Alternative Titles

Full title

Structural basis of tubulin detyrosination by VASH2/SVBP heterodimer

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_73149a2dc2634b788e4b85463c6af74a

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_73149a2dc2634b788e4b85463c6af74a

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-019-11277-8

How to access this item